ID   PDIA4_HUMAN             Reviewed;         645 AA.
AC   P13667; A8K4K6; Q549T6;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   02-SEP-2026, entry version 247.
DE   RecName: Full=Protein disulfide-isomerase A4;
DE            EC=5.3.4.1 {ECO:0000250|UniProtKB:P08003};
DE   AltName: Full=Endoplasmic reticulum resident protein 70;
DE            Short=ER protein 70;
DE            Short=ERp70;
DE   AltName: Full=Endoplasmic reticulum resident protein 72;
DE            Short=ER protein 72;
DE            Short=ERp-72;
DE            Short=ERp72;
DE   Flags: Precursor;
GN   Name=PDIA4; Synonyms=ERP70, ERP72;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2549034; DOI=10.1016/s0021-9258(18)63764-0;
RA   Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
RT   "Human deoxycytidine kinase. Sequence of cDNA clones and analysis of
RT   expression in cell lines with and without enzyme activity.";
RL   J. Biol. Chem. 264:14762-14768(1989).
RN   [2]
RP   ERRATUM OF PUBMED:2549034, AND SEQUENCE REVISION.
RX   PubMed=2002068; DOI=10.1016/s0021-9258(19)67795-1;
RA   Huang S.-H., Tomich J.M., Wu H., Jong A., Holcenberg J.S.;
RL   J. Biol. Chem. 266:5353-5353(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung, and Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   COMPONENT OF A CHAPERONE COMPLEX.
RX   PubMed=12475965; DOI=10.1091/mbc.e02-05-0311;
RA   Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT   "A subset of chaperones and folding enzymes form multiprotein complexes in
RT   endoplasmic reticulum to bind nascent proteins.";
RL   Mol. Biol. Cell 13:4456-4469(2002).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=12643545; DOI=10.1021/pr025562r;
RA   Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA   Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA   Appella E.;
RT   "Proteomic analysis of early melanosomes: identification of novel
RT   melanosomal proteins.";
RL   J. Proteome Res. 2:69-79(2003).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   TISSUE=Melanoma;
RX   PubMed=17081065; DOI=10.1021/pr060363j;
RA   Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA   Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA   Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT   "Proteomic and bioinformatic characterization of the biogenesis and
RT   function of melanosomes.";
RL   J. Proteome Res. 5:3135-3144(2006).
RN   [10]
RP   INTERACTION WITH HUMAN ASTROVIRUS-1 AND HUMAN ASTROVIRUS-1 SPIKE PROTEIN
RP   VP25 (MICROBIAL INFECTION).
RX   PubMed=33396308; DOI=10.3390/v13010053;
RA   Aguilar-Hernandez N., Meyer L., Lopez S., DuBois R.M., Arias C.F.;
RT   "Protein Disulfide Isomerase A4 Is Involved in Genome Uncoating during
RT   Human Astrovirus Cell Entry.";
RL   Viruses 13:0-0(2020).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-366, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 53-284.
RX   PubMed=20600112; DOI=10.1016/j.jmb.2010.06.045;
RA   Kozlov G., Azeroual S., Rosenauer A., Maeaettaenen P., Denisov A.Y.,
RA   Thomas D.Y., Gehring K.;
RT   "Structure of the catalytic a(0)a fragment of the protein disulfide
RT   isomerase ERp72.";
RL   J. Mol. Biol. 401:618-625(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC         EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:P08003};
CC   -!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
CC       DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGGT1
CC       and very small amounts of ERP29, but not, or at very low levels, CALR
CC       nor CANX. Component of a complex containing at least CRELD2, MANF,
CC       MATN3 and PDIA4 (By similarity). {ECO:0000250|UniProtKB:P08003}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with Human astrovirus-1 and
CC       Human astrovirus-8 spike protein VP25; this interaction seems to
CC       facilitate the uncoating during virus entry into the cell
CC       (PubMed:33396308). Does not interact with Human astrovirus-2 spike
CC       protein VP25 (PubMed:33396308). {ECO:0000269|PubMed:33396308}.
CC   -!- INTERACTION:
CC       P13667; Q9NPA0: EMC7; NbExp=2; IntAct=EBI-1054653, EBI-6309137;
CC       P13667; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1054653, EBI-10171774;
CC       P13667; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-1054653, EBI-10210845;
CC       P13667; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-1054653, EBI-10302392;
CC       P13667; P80188: LCN2; NbExp=3; IntAct=EBI-1054653, EBI-11911016;
CC       P13667; O15232: MATN3; NbExp=6; IntAct=EBI-1054653, EBI-6262458;
CC       P13667; P23284: PPIB; NbExp=2; IntAct=EBI-1054653, EBI-359252;
CC       P13667; PRO_0000025479 [P23284]: PPIB; NbExp=3; IntAct=EBI-1054653, EBI-8771982;
CC       P13667; Q76353; Xeno; NbExp=3; IntAct=EBI-1054653, EBI-6248077;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:12643545}. Melanosome
CC       {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in
CC       melanosome fractions from stage I to stage IV (PubMed:17081065).
CC       {ECO:0000269|PubMed:17081065}.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be a deoxycytidine kinase.
CC       {ECO:0000305|PubMed:2549034}.
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DR   EMBL; J05016; AAA58460.1; -; mRNA.
DR   EMBL; AK290971; BAF83660.1; -; mRNA.
DR   EMBL; AC093743; AAQ96863.1; -; Genomic_DNA.
DR   EMBL; CH471146; EAW80065.1; -; Genomic_DNA.
DR   EMBL; CH471146; EAW80066.1; -; Genomic_DNA.
DR   EMBL; BC000425; AAH00425.1; -; mRNA.
DR   EMBL; BC001928; AAH01928.1; -; mRNA.
DR   EMBL; BC006344; AAH06344.1; -; mRNA.
DR   EMBL; BC011754; AAH11754.1; -; mRNA.
DR   CCDS; CCDS5893.1; -.
DR   PIR; A23723; A23723.
DR   RefSeq; NP_004902.1; NM_004911.5.
DR   PDB; 3IDV; X-ray; 1.95 A; A=53-284.
DR   AlphaFoldDB; P13667; -.
DR   SMR; P13667; -.
DR   BioGRID; 114966; 537.
DR   FunCoup; P13667; 326.
DR   IntAct; P13667; 175.
DR   MINT; P13667; -.
DR   NDEx; IQUERY-CP-PDIA4; 2 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000499129; -.
DR   BindingDB; P13667; -.
DR   ChEMBL; CHEMBL4295717; -.
DR   GlyGen; P13667; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; P13667; -.
DR   MetOSite; P13667; -.
DR   PhosphoSitePlus; P13667; -.
DR   SwissPalm; P13667; -.
DR   BioMuta; PDIA4; -.
DR   DMDM; 119530; -.
DR   OGP; P13667; -.
DR   REPRODUCTION-2DPAGE; IPI00009904; -.
DR   CPTAC; CPTAC-105; -.
DR   CPTAC; CPTAC-106; -.
DR   jPOST; P13667; -.
DR   MassIVE; P13667; -.
DR   PaxDb; 9606-ENSP00000499129; -.
DR   PeptideAtlas; P13667; -.
DR   ProteomicsDB; 52955; -.
DR   Pumba; P13667; -.
DR   Antibodypedia; 3377; 522 antibodies from 35 providers.
DR   DNASU; 9601; -.
DR   Ensembl; ENST00000652332.1; ENSP00000499129.1; ENSG00000155660.12.
DR   GeneID; 9601; -.
DR   KEGG; hsa:9601; -.
DR   MANE-Select; ENST00000652332.1; ENSP00000499129.1; NM_004911.5; NP_004902.1.
DR   UCSC; uc003wff.3; human.
DR   AGR; HGNC:30167; -.
DR   ClinPGx; PA142671190; -.
DR   CTD; 9601; -.
DR   DisGeNET; 9601; -.
DR   GeneCards; PDIA4; -.
DR   HGNC; HGNC:30167; PDIA4.
DR   HPA; ENSG00000155660; Low tissue specificity.
DR   MIM; 620018; gene.
DR   OpenTargets; ENSG00000155660; -.
DR   VEuPathDB; HostDB:ENSG00000155660; -.
DR   eggNOG; KOG0190; Eukaryota.
DR   GeneTree; ENSGT00940000157738; -.
DR   HOGENOM; CLU_025879_6_2_1; -.
DR   InParanoid; P13667; -.
DR   OMA; FRSKHEP; -.
DR   OrthoDB; 427280at2759; -.
DR   PAN-GO; P13667; 5 GO annotations based on evolutionary models.
DR   PhylomeDB; P13667; -.
DR   BRENDA; 5.3.4.1; 2681.
DR   PathwayCommons; P13667; -.
DR   SignaLink; P13667; -.
DR   Agora; ENSG00000155660; -.
DR   BioGRID-ORCS; 9601; 10 hits in 1153 CRISPR screens.
DR   ChiTaRS; PDIA4; human.
DR   EvolutionaryTrace; P13667; -.
DR   GenomeRNAi; 9601; -.
DR   Pharos; P13667; Tbio.
DR   PRO; PR:P13667; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P13667; protein.
DR   Bgee; ENSG00000155660; Expressed in pylorus and 205 other cell types or tissues.
DR   ExpressionAtlas; P13667; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; EXP:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0042470; C:melanosome; EXP:UniProtKB.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; ISS:UniProtKB.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR   GO; GO:0009306; P:protein secretion; TAS:ProtInc.
DR   CDD; cd02961; PDI_a_family; 2.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd03073; PDI_b'_ERp72_ERp57; 1.
DR   CDD; cd03068; PDI_b_ERp72; 1.
DR   FunFam; 3.40.30.10:FF:000017; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.40.30.10:FF:000067; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.40.30.10:FF:000076; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.40.30.10:FF:000084; Protein disulfide-isomerase A4; 1.
DR   FunFam; 3.40.30.10:FF:000126; Protein disulfide-isomerase A4; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 5.
DR   InterPro; IPR005788; PDI_thioredoxin-like_dom.
DR   InterPro; IPR041866; PDIA4_PDI_b.
DR   InterPro; IPR005792; Prot_disulphide_isomerase.
DR   InterPro; IPR017068; Protein_diS-isomerase_A4.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01130; ER_PDI_fam; 1.
DR   NCBIfam; TIGR01126; pdi_dom; 3.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF210; PROTEIN DISULFIDE-ISOMERASE A4; 1.
DR   Pfam; PF00085; Thioredoxin; 3.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   PIRSF; PIRSF036862; Disulphide_isom_A4; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 5.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 3.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
DR   PDBsum; 3IDV; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW   Endoplasmic reticulum; Host-virus interaction; Isomerase;
KW   Proteomics identification; Redox-active center; Reference proteome; Repeat;
KW   Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..645
FT                   /note="Protein disulfide-isomerase A4"
FT                   /id="PRO_0000034229"
FT   DOMAIN          21..169
FT                   /note="Thioredoxin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          158..301
FT                   /note="Thioredoxin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DOMAIN          505..636
FT                   /note="Thioredoxin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   REGION          24..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           91..94
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250|UniProtKB:P08003"
FT   MOTIF           555..558
FT                   /note="CXXC"
FT                   /evidence="ECO:0000250|UniProtKB:P08003"
FT   MOTIF           642..645
FT                   /note="Prevents secretion from ER"
FT   COMPBIAS        38..58
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         366
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   DISULFID        91..94
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P08003,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        206..209
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        555..558
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250|UniProtKB:P08003,
FT                   ECO:0000255|PROSITE-ProRule:PRU00691"
FT   VARIANT         173
FT                   /note="T -> M (in dbSNP:rs2290971)"
FT                   /id="VAR_052580"
FT   CONFLICT        102
FT                   /note="E -> G (in Ref. 3; BAF83660)"
FT                   /evidence="ECO:0000305"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           72..76
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          80..87
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           92..109
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          117..121
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           126..131
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          136..144
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           157..168
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           174..177
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   TURN            184..186
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           187..193
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          195..202
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           208..211
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           213..224
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          226..228
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          232..236
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   TURN            237..239
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           241..246
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          251..259
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   STRAND          262..265
FT                   /evidence="ECO:0007829|PDB:3IDV"
FT   HELIX           272..282
FT                   /evidence="ECO:0007829|PDB:3IDV"
SQ   SEQUENCE   645 AA;  72932 MW;  1919C2AE12CD2684 CRC64;
     MRPRKAFLLL LLLGLVQLLA VAGAEGPDED SSNRENAIED EEEEEEEDDD EEEDDLEVKE
     ENGVLVLNDA NFDNFVADKD TVLLEFYAPW CGHCKQFAPE YEKIANILKD KDPPIPVAKI
     DATSASVLAS RFDVSGYPTI KILKKGQAVD YEGSRTQEEI VAKVREVSQP DWTPPPEVTL
     VLTKENFDEV VNDADIILVE FYAPWCGHCK KLAPEYEKAA KELSKRSPPI PLAKVDATAE
     TDLAKRFDVS GYPTLKIFRK GRPYDYNGPR EKYGIVDYMI EQSGPPSKEI LTLKQVQEFL
     KDGDDVIIIG VFKGESDPAY QQYQDAANNL REDYKFHHTF STEIAKFLKV SQGQLVVMQP
     EKFQSKYEPR SHMMDVQGST QDSAIKDFVL KYALPLVGHR KVSNDAKRYT RRPLVVVYYS
     VDFSFDYRAA TQFWRSKVLE VAKDFPEYTF AIADEEDYAG EVKDLGLSES GEDVNAAILD
     ESGKKFAMEP EEFDSDTLRE FVTAFKKGKL KPVIKSQPVP KNNKGPVKVV VGKTFDSIVM
     DPKKDVLIEF YAPWCGHCKQ LEPVYNSLAK KYKGQKGLVI AKMDATANDV PSDRYKVEGF
     PTIYFAPSGD KKNPVKFEGG DRDLEHLSKF IEEHATKLSR TKEEL
//